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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/3310

Title: Microbial nitrilases: versatile, spiral forming, industrial enzymes
Authors: Thuku, RN
Brady, D
Benedik, MJ
Sewell, BT
Keywords: Nitrilase
Helical enzymes
Spiral enzymes
Nitrilase superfamily
Microbial nitrilases
Industrial enzymes
Issue Date: Mar-2009
Publisher: Blackwell Publishing
Citation: Thuku, RN, Brady, D, Benedik, MJ and Sewell, BT. 2009. Microbial nitrilases: versatile, spiral forming, industrial enzymes. Journal of Applied Microbiology, Vol. 106(3), pp 1-48
Abstract: The nitrilases are enzymes that convert nitriles to the corresponding acid and ammonia. They are members of a superfamily, which includes amidases and occur in both prokaryotes and eukaryotes. The superfamily is characterized by having a homodimeric building block with a abba–abba sandwich fold and an active site containing four positionally conserved residues: cys, glu, glu and lys. Their high chemical specificity and frequent enantioselectivity makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation. The superfamily enzymes have been visualized as dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers and variable length helices, but all nitrilase oligomers have the same basic dimer interface. Moreover, in the case of the octamers, tetradecamers, octadecamers and the helices, common principles of subunit association apply. While the range of industrially interesting reactions catalysed by this enzyme class continues to increase, research efforts are still hampered by the lack of a high resolution microbial nitrilase structure which can provide insights into their specificity, enantioselectivity and the mechanism of catalysis. This review provides an overview of the current progress in elucidation of structure and function in this enzyme class and emphasizes insights that may lead to further biotechnological application
Description: Copyright: 2008 Blackwell Publishing
URI: http://hdl.handle.net/10204/3310
ISSN: 1364-5072
Appears in Collections:Enzyme technologies
General science, engineering & technology

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